Reviewed, UniProtKB/Swiss-Prot Q63755 (PRDM2_RAT)

Names and origin

Protein names

Recommended name:
    PR domain zinc finger protein 2
    EC=2.1.1.43
Alternative name(s):
    PR domain-containing protein 2
    Retinoblastoma protein-interacting zinc finger protein
    Zinc finger protein RIZ

Gene names

Name:	Prdm2
Synonyms:	Riz

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1706 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3. May function as a DNA-binding transcription factor. Binds to the macrophage-specific TPA-responsive element (MTE) of the HMOX1 (heme oxygenase 1) gene and may act as a transcriptional activator of this gene By similarity.
Catalytic activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
Subunit structure	Binds to the retinoblastoma protein (RB). Interacts with GATA3 By similarity.
Subcellular location	Nucleus By similarity.
Sequence similarities	Contains 8 C2H2-type zinc fingers. Contains 1 SET domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Methyltransferase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW histone-lysine N-methyltransferase activity Inferred from electronic annotation. Source: EC transcription regulator activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1706	1706	PR domain zinc finger protein 2		PRO_0000047759
Regions
	Domain	26 – 144	119	SET
	Zinc finger	355 – 377	23	C2H2-type 1
	Zinc finger	385 – 407	23	C2H2-type 2
	Zinc finger	476 – 499	24	C2H2-type 3
	Zinc finger	1123 – 1145	23	C2H2-type 4
	Zinc finger	1151 – 1174	24	C2H2-type 5
	Zinc finger	1180 – 1203	24	C2H2-type 6
	Zinc finger	1321 – 1343	23	C2H2-type 7; atypical
	Zinc finger	1443 – 1465	23	C2H2-type 8; atypical
	Compositional bias	246 – 327	82	Glu-rich
	Compositional bias	893 – 1067	175	Pro-rich
	Compositional bias	1472 – 1565	94	Ser-rich
Amino acid modifications
	Modified residue	637	1	Phosphoserine By similarity
	Modified residue	734	1	Phosphoserine By similarity
	Modified residue	738	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q63755-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 55EA419491D2D68C	FASTA	1,706	187,555
	10 20 30 40 50 60 MHQNTESVAA TETLAEVPEH VLRGLPEEVR LFPSAVDKTR IGVWATKPIL KGKKFGPFVG 70 80 90 100 110 120 DKKKRSQVRN NVYMWEVYYP NLGWMCIDAT DPEKGNWLRY VNWACSGEEQ NLFPLEINRA 130 140 150 160 170 180 IYYKTLKPIA PGEELLVWYN GEDNPEIAAA IEEERASARS KRSSPKSRRG KKKSHENKNK 190 200 210 220 230 240 GIRTHPTQLK ASELDSTFAN MRGSAEGPKE EDERPLASAP EQPAPLPEVG NQDAVPQVAI 250 260 270 280 290 300 PLPACEPQPE VDGKQEVTDC EVNDVEEEEL EEEEELEEEE EEELGEDGVE EADMPNESSA 310 320 330 340 350 360 KEPEIRCEEK PEDLLEEPQS MSNEAREDSP DVTPPPHTPR AREEANGDVL ETFMFPCQHC 370 380 390 400 410 420 ERKFATKQGL ERHMHIHIST INHAFKCKYC GKRFGTQINR RRHERRHETG LKRRPSMTLQ 430 440 450 460 470 480 SSEDPDDGKG ENVTSKDESS PPQLGQDCLI LNSEKTSQEV LNSSFVEENG EVKELHPCKY 490 500 510 520 530 540 CKKVFGTHTN MRRHQRRVHE RHLIPKGVRR KGGLLEEPQP PAEQAPPSQN VYVPSTEPEE 550 560 570 580 590 600 EGETDDVYIM DISSNISENL NYYIDGKIQT NSSTSNCDVI EMESNSAHLY GIDCLLTPVT 610 620 630 640 650 660 VEITQNIKST QVSVTDDLLK DSPSSTNCES KKRRTASPPV LPKIKTETES DSTAPSCSLS 670 680 690 700 710 720 LPLSISTAEV VSFHKEKGVY LSSKLKQLLQ TQDKLTLPAG FSAAEIPKLG PVCASAPASM 730 740 750 760 770 780 LPVTSSRFKR RTSSPPSSPQ HSPALRDFGK PNDGKAAWTD TVLTSKKPKL ESRSDSPAWS 790 800 810 820 830 840 LSGRDERETG SPPCFDEYKI SKEWAASSTF SSVCNQQPLD LSSGVKQKSE GTGKTPVPWE 850 860 870 880 890 900 SVLDLSVHKK PCDSEGKEFK ENHLAQPAAK KKKPTTCMLQ KVLLNEYNGV SLPTETTPEV 910 920 930 940 950 960 TRSPSPCKSP DTQPDPELGP DSSCSVPTAE SPPEVVGPSS PPLQTASLSS GQLPPLLTPT 970 980 990 1000 1010 1020 EPSSPPPCPP VLTVATPPPP LLPTVPLSHP SSDASPQQCP SPFSNTTAQS PLPILSPTVS 1030 1040 1050 1060 1070 1080 PSPSPIPPVE PLMSAASPGP PTLSSSSSSS SSFPSSSCSS TSPSPPPLSA VSSVVSSGDN 1090 1100 1110 1120 1130 1140 LEASLPAVTF KQEESESEGL KPKEEAPPAG GQSVVQETFS KNFICNVCES PFLSIKDLTK 1150 1160 1170 1180 1190 1200 HLSVHAEEWP FKCEFCVQLF KVKTDLSEHR FLLHGVGNIF VCSVCKKEFA FLCNLQQHQR 1210 1220 1230 1240 1250 1260 DLHPDEVCTH HEFESGTLRP QNFTDPSKAN VEHMPSLPEE PLETSREEEL NDSSEELYTT 1270 1280 1290 1300 1310 1320 IKIMASGIKT KDPDVRLGLN QHYPSFKPPP FQYHHRNPMG IGVTATNFTT HNIPQTFTTA 1330 1340 1350 1360 1370 1380 IRCTKCGKGV DNMPELHKHI LACASASDKK RYTPKKNPVP LKQTVQPKNG VVVLDNSGKN 1390 1400 1410 1420 1430 1440 AFRRMGQPKR LSFNVELGKM SPNKLKLSAL KKKNQLVQKA ILQKNRAAKQ KADLRDTSEA 1450 1460 1470 1480 1490 1500 SSHICPYCDR EFTYIGSLNK HAAFSCPKKP LSPSKRKVSH SSKKGGHASS SSSDRNSSCH 1510 1520 1530 1540 1550 1560 PRRRTADTEI KMQSTQAPLG KTRARSTGPA QASLPSSSFR SRQNVKFAAS VKSKKASSSS 1570 1580 1590 1600 1610 1620 LRNSSPIRMA KITHVEGKKP KAVAKSHSAQ LSSKSSRGLH VRVQKSKAVI QSKTALASKR 1630 1640 1650 1660 1670 1680 RTDRFIVKSR ERSGGPITRS LQLAAAADLS ESRREDSSAR HELKDFSYSL RLASRCGSST 1690 1700 ASYITRQCRK VKAAAATPFQ GPFLKE

References

[1]	"The retinoblastoma protein binds to RIZ, a zinc-finger protein that shares an epitope with the adenovirus E1A protein." Buyse I.M., Shao G., Huang S. Proc. Natl. Acad. Sci. U.S.A. 92:4467-4471(1995) [PubMed: 7538672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U17837 mRNA. Translation: AAA74468.1.
IPI	IPI00327589.
RefSeq	NP_001071116.1.
UniGene	Rn.202632
3D structure databases
SMR	Q63755. Positions 1-160, 354-500, 1121-1206.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-473N.
STRING	Q63755.
PTM databases
PhosphoSite	Q63755.
Genome annotation databases
Ensembl	ENSRNOT00000041175; ENSRNOP00000046011; ENSRNOG00000033522; Rattus norvegicus. [Genome view]
GeneID	313678.
KEGG	rno:313678.
UCSC	U17837. rat.
Organism-specific databases
CTD	313678.
RGD	1594531. Prdm2.
Phylogenomic databases
eggNOG	roNOG04288.
HOVERGEN	Q63755.
InParanoid	Q63755.
Gene expression databases
ArrayExpress	Q63755.
Genevestigator	Q63755.
GermOnline	ENSRNOG00000033522. Rattus norvegicus.
Family and domain databases
InterPro	IPR009170. RIZ_retinblastoma-bd_prot. IPR001214. SET_dom. IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. [Graphical view]
Pfam	PF00856. SET. 1 hit. [Graphical view]
PIRSF	PIRSF002395. RIZ_SET. 1 hit.
SMART	SM00317. SET. 1 hit. SM00355. ZnF_C2H2. 8 hits. [Graphical view]
PROSITE	PS50280. SET. 1 hit. PS00028. ZINC_FINGER_C2H2_1. 6 hits. PS50157. ZINC_FINGER_C2H2_2. 7 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	666643.

Entry information

Entry name

PRDM2_RAT

Accession

Primary (citable) accession number: Q63755

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 21, 2004
Last sequence update:	November 1, 1996
Last modified:	February 9, 2010
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)